Phosphorylation of CREB at Ser-133 induces complex formation with CREB-binding protein via a direct mechanism.

We have characterized a phosphoserine binding domain in the coactivator CREB-binding protein (CBP) which interacts with the protein kinase A-phosphorylated, and hence activated, form of the cyclic AMP-responsive factor CREB. The CREB binding domain, referred to as KIX, is alpha helical and binds to...

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Publicat a:	Mol Cell Biol
Autors principals:	Parker, D, Ferreri, K, Nakajima, T, LaMorte, V J, Evans, R, Koerber, S C, Hoeger, C, Montminy, M R
Format:	Artigo
Idioma:	Inglês
Publicat:	Taylor & Francis 1996
Matèries:	Research Article
Accés en línia:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC231049/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8552098/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/mcb.16.2.694
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